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Conserved domains on  [gi|1107030588|emb|SGB67206|]
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peroxidoxin [Mycobacterium tuberculosis]

Protein Classification

peroxiredoxin( domain architecture ID 10122458)

peroxiredoxin belonging to the bacterioferritin comigratory protein (BCP) subfamily is a thioredoxin-dependent thiol-specific peroxidase that catalyzes the reduction of hydrogen peroxide and organic hydroperoxides to water and alcohols, respectively

CATH:  3.40.30.10
EC:  1.11.1.24
Gene Ontology:  GO:0051920|GO:0008379
PubMed:  15518547|12517450|10644761|15558583
SCOP:  4000042

Graphical summary

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List of domain hits

 Name Accession Description Interval E-value
PRX_BCP cd03017
Peroxiredoxin (PRX) family, Bacterioferritin comigratory protein (BCP) subfamily; composed of ...
 5-146 6.89e-56

Peroxiredoxin (PRX) family, Bacterioferritin comigratory protein (BCP) subfamily; composed of thioredoxin-dependent thiol peroxidases, widely expressed in pathogenic bacteria, that protect cells against toxicity from reactive oxygen species by reducing and detoxifying hydroperoxides. The protein was named BCP based on its electrophoretic mobility before its function was known. BCP shows substrate selectivity toward fatty acid hydroperoxides rather than hydrogen peroxide or alkyl hydroperoxides. BCP contains the peroxidatic cysteine but appears not to possess a resolving cysteine (some sequences, not all, contain a second cysteine but its role is still unknown). Unlike other PRXs, BCP exists as a monomer. The plant homolog of BCP is PRX Q, which is expressed only in leaves and is cellularly localized in the chloroplasts and the guard cells of stomata. Also included in this subfamily is the fungal nuclear protein, Dot5p (for disrupter of telomere silencing protein 5), which functions as an alkyl-hydroperoxide reductase during post-diauxic growth.


:

Pssm-ID: 239315  Cd Length: 140  Bit Score: 171.58  E-value: 6.89e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1107030588   5 DTVADFELPDQTGTPRRLSVLLSdGPVVLFFYPAAMTPGCTKEACHFRDLAKEFAEVRASRVGISTDPVRKQAKFAEVRR 84
Cdd:cd03017     1 DKAPDFTLPDQDGETVSLSDLRG-KPVVLYFYPKDDTPGCTKEACDFRDLYEEFKALGAVVIGVSPDSVESHAKFAEKYG 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1107030588  85 FDYPLLSDAQGTVAAQFGVKRGLLGKLMPVKRTTFVIDTDRKVLDVISSeFSMDAHADKALA 146
Cdd:cd03017    80 LPFPLLSDPDGKLAKAYGVWGEKKKKYMGIERSTFLIDPDGKIVKVWRK-VKPKGHAEEVLE 140
 
Name Accession Description Interval E-value
PRX_BCP cd03017
Peroxiredoxin (PRX) family, Bacterioferritin comigratory protein (BCP) subfamily; composed of ...
 5-146 6.89e-56

Peroxiredoxin (PRX) family, Bacterioferritin comigratory protein (BCP) subfamily; composed of thioredoxin-dependent thiol peroxidases, widely expressed in pathogenic bacteria, that protect cells against toxicity from reactive oxygen species by reducing and detoxifying hydroperoxides. The protein was named BCP based on its electrophoretic mobility before its function was known. BCP shows substrate selectivity toward fatty acid hydroperoxides rather than hydrogen peroxide or alkyl hydroperoxides. BCP contains the peroxidatic cysteine but appears not to possess a resolving cysteine (some sequences, not all, contain a second cysteine but its role is still unknown). Unlike other PRXs, BCP exists as a monomer. The plant homolog of BCP is PRX Q, which is expressed only in leaves and is cellularly localized in the chloroplasts and the guard cells of stomata. Also included in this subfamily is the fungal nuclear protein, Dot5p (for disrupter of telomere silencing protein 5), which functions as an alkyl-hydroperoxide reductase during post-diauxic growth.


Pssm-ID: 239315  Cd Length: 140  Bit Score: 171.58  E-value: 6.89e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1107030588   5 DTVADFELPDQTGTPRRLSVLLSdGPVVLFFYPAAMTPGCTKEACHFRDLAKEFAEVRASRVGISTDPVRKQAKFAEVRR 84
Cdd:cd03017     1 DKAPDFTLPDQDGETVSLSDLRG-KPVVLYFYPKDDTPGCTKEACDFRDLYEEFKALGAVVIGVSPDSVESHAKFAEKYG 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1107030588  85 FDYPLLSDAQGTVAAQFGVKRGLLGKLMPVKRTTFVIDTDRKVLDVISSeFSMDAHADKALA 146
Cdd:cd03017    80 LPFPLLSDPDGKLAKAYGVWGEKKKKYMGIERSTFLIDPDGKIVKVWRK-VKPKGHAEEVLE 140
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
9-148 1.25e-40

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 132.68  E-value: 1.25e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1107030588   9 DFELPDQTGTPRRLSVLLSDgPVVLFFYpAAMTPGCTKEACHFRDLAKEFAEVRASRVGISTDPVRKQAKFAEVRRFDYP 88
Cdd:COG1225     3 DFTLPDLDGKTVSLSDLRGK-PVVLYFY-ATWCPGCTAELPELRDLYEEFKDKGVEVLGVSSDSDEAHKKFAEKYGLPFP 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1107030588  89 LLSDAQGTVAAQFGVKRgllgklmpvKRTTFVIDTDRKVLDVISSEFSMDAHADKALATL 148
Cdd:COG1225    81 LLSDPDGEVAKAYGVRG---------TPTTFLIDPDGKIRYVWVGPVDPRPHLEEVLEAL 131
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 4-127 4.67e-39

AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) and thiol specific antioxidant (TSA).


Pssm-ID: 425763 [Multi-domain]  Cd Length: 124  Bit Score: 128.50  E-value: 4.67e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1107030588   4 GDTVADFELPDQTGTPRRLSVLLsDGPVVLFFYPAAMTPGCTKEACHFRDLAKEFAEVRASRVGISTDPVRKQAKFAEVR 83
Cdd:pfam00578   2 GDKAPDFELPDGDGGTVSLSDYR-GKWVVLFFYPADWTPVCTTELPALADLYEEFKKLGVEVLGVSVDSPESHKAFAEKY 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1107030588  84 RFDYPLLSDAQGTVAAQFGVKRgllGKLMPVKRTTFVIDTDRKV 127
Cdd:pfam00578  81 GLPFPLLSDPDGEVARAYGVLN---EEEGGALRATFVIDPDGKV 121
bcp PRK09437
thioredoxin-dependent thiol peroxidase; Reviewed
 1-130 2.55e-33

thioredoxin-dependent thiol peroxidase; Reviewed


Pssm-ID: 181857  Cd Length: 154  Bit Score: 114.65  E-value: 2.55e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1107030588   1 MKTGDTVADFELPDQTGTPrrlsVLLSD---GPVVLFFYPAAMTPGCTKEACHFRDLAKEFAEVRASRVGISTDPVRKQA 77
Cdd:PRK09437    4 LKAGDIAPKFSLPDQDGEQ----VSLTDfqgQRVLVYFYPKAMTPGCTVQACGLRDNMDELKKAGVVVLGISTDKPEKLS 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1107030588  78 KFAEVRRFDYPLLSDAQGTVAAQFGV--KRGLLGKLMP-VKRTTFVIDTDRKVLDV 130
Cdd:PRK09437   80 RFAEKELLNFTLLSDEDHQVAEQFGVwgEKKFMGKTYDgIHRISFLIDADGKIEHV 135
 
Name Accession Description Interval E-value
PRX_BCP cd03017
Peroxiredoxin (PRX) family, Bacterioferritin comigratory protein (BCP) subfamily; composed of ...
 5-146 6.89e-56

Peroxiredoxin (PRX) family, Bacterioferritin comigratory protein (BCP) subfamily; composed of thioredoxin-dependent thiol peroxidases, widely expressed in pathogenic bacteria, that protect cells against toxicity from reactive oxygen species by reducing and detoxifying hydroperoxides. The protein was named BCP based on its electrophoretic mobility before its function was known. BCP shows substrate selectivity toward fatty acid hydroperoxides rather than hydrogen peroxide or alkyl hydroperoxides. BCP contains the peroxidatic cysteine but appears not to possess a resolving cysteine (some sequences, not all, contain a second cysteine but its role is still unknown). Unlike other PRXs, BCP exists as a monomer. The plant homolog of BCP is PRX Q, which is expressed only in leaves and is cellularly localized in the chloroplasts and the guard cells of stomata. Also included in this subfamily is the fungal nuclear protein, Dot5p (for disrupter of telomere silencing protein 5), which functions as an alkyl-hydroperoxide reductase during post-diauxic growth.


Pssm-ID: 239315  Cd Length: 140  Bit Score: 171.58  E-value: 6.89e-56
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1107030588   5 DTVADFELPDQTGTPRRLSVLLSdGPVVLFFYPAAMTPGCTKEACHFRDLAKEFAEVRASRVGISTDPVRKQAKFAEVRR 84
Cdd:cd03017     1 DKAPDFTLPDQDGETVSLSDLRG-KPVVLYFYPKDDTPGCTKEACDFRDLYEEFKALGAVVIGVSPDSVESHAKFAEKYG 79

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1107030588  85 FDYPLLSDAQGTVAAQFGVKRGLLGKLMPVKRTTFVIDTDRKVLDVISSeFSMDAHADKALA 146
Cdd:cd03017    80 LPFPLLSDPDGKLAKAYGVWGEKKKKYMGIERSTFLIDPDGKIVKVWRK-VKPKGHAEEVLE 140
Bcp COG1225
Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];
9-148 1.25e-40

Peroxiredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440838 [Multi-domain]  Cd Length: 136  Bit Score: 132.68  E-value: 1.25e-40
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1107030588   9 DFELPDQTGTPRRLSVLLSDgPVVLFFYpAAMTPGCTKEACHFRDLAKEFAEVRASRVGISTDPVRKQAKFAEVRRFDYP 88
Cdd:COG1225     3 DFTLPDLDGKTVSLSDLRGK-PVVLYFY-ATWCPGCTAELPELRDLYEEFKDKGVEVLGVSSDSDEAHKKFAEKYGLPFP 80

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|
gi 1107030588  89 LLSDAQGTVAAQFGVKRgllgklmpvKRTTFVIDTDRKVLDVISSEFSMDAHADKALATL 148
Cdd:COG1225    81 LLSDPDGEVAKAYGVRG---------TPTTFLIDPDGKIRYVWVGPVDPRPHLEEVLEAL 131
AhpC-TSA pfam00578
AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) ...
 4-127 4.67e-39

AhpC/TSA family; This family contains proteins related to alkyl hydroperoxide reductase (AhpC) and thiol specific antioxidant (TSA).


Pssm-ID: 425763 [Multi-domain]  Cd Length: 124  Bit Score: 128.50  E-value: 4.67e-39
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1107030588   4 GDTVADFELPDQTGTPRRLSVLLsDGPVVLFFYPAAMTPGCTKEACHFRDLAKEFAEVRASRVGISTDPVRKQAKFAEVR 83
Cdd:pfam00578   2 GDKAPDFELPDGDGGTVSLSDYR-GKWVVLFFYPADWTPVCTTELPALADLYEEFKKLGVEVLGVSVDSPESHKAFAEKY 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....
gi 1107030588  84 RFDYPLLSDAQGTVAAQFGVKRgllGKLMPVKRTTFVIDTDRKV 127
Cdd:pfam00578  81 GLPFPLLSDPDGEVARAYGVLN---EEEGGALRATFVIDPDGKV 121
PRX_family cd02971
Peroxiredoxin (PRX) family; composed of the different classes of PRXs including many proteins ...
 9-145 3.68e-37

Peroxiredoxin (PRX) family; composed of the different classes of PRXs including many proteins originally known as bacterioferritin comigratory proteins (BCP), based on their electrophoretic mobility before their function was identified. PRXs are thiol-specific antioxidant (TSA) proteins also known as TRX peroxidases and alkyl hydroperoxide reductase C22 (AhpC) proteins. They confer a protective antioxidant role in cells through their peroxidase activity in which hydrogen peroxide, peroxynitrate, and organic hydroperoxides are reduced and detoxified using reducing equivalents derived from either TRX, glutathione, trypanothione and AhpF. They are distinct from other peroxidases in that they have no cofactors such as metals or prosthetic groups. The first step of catalysis, common to all PRXs, is the nucleophilic attack by the catalytic cysteine (also known as the peroxidatic cysteine) on the peroxide leading to cleavage of the oxygen-oxygen bond and the formation of a cysteine sulfenic acid intermediate. The second step of the reaction, the resolution of the intermediate, distinguishes the different types of PRXs. The presence or absence of a second cysteine (the resolving cysteine) classifies PRXs as either belonging to the 2-cys or 1-cys type. The resolving cysteine of 2-cys PRXs is either on the same chain (atypical) or on the second chain (typical) of a functional homodimer. Structural and motif analysis of this growing family supports the need for a new classification system. The peroxidase activity of PRXs is regulated in vivo by irreversible cysteine over-oxidation into a sulfinic acid, phosphorylation and limited proteolysis.


Pssm-ID: 239269 [Multi-domain]  Cd Length: 140  Bit Score: 124.20  E-value: 3.68e-37
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1107030588   9 DFELPDQTGTPRRLSVLLsDGPVVLFFYPAAMTPGCTKEACHFRDLAKEFAEVRASRVGISTDPVRKQAKFAEV-RRFDY 87
Cdd:cd02971     4 DFTLPATDGGEVSLSDFK-GKWVVLFFYPKDFTPVCTTELCAFRDLAEEFAKGGAEVLGVSVDSPFSHKAWAEKeGGLNF 82

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*...
gi 1107030588  88 PLLSDAQGTVAAQFGVKRGLLGKLMPVKRTTFVIDTDRKVLDVISSEFSmDAHADKAL 145
Cdd:cd02971    83 PLLSDPDGEFAKAYGVLIEKSAGGGLAARATFIIDPDGKIRYVEVEPLP-TGRNAEEL 139
PRX_AhpE_like cd03018
Peroxiredoxin (PRX) family, AhpE-like subfamily; composed of proteins similar to Mycobacterium ...
 1-127 7.77e-36

Peroxiredoxin (PRX) family, AhpE-like subfamily; composed of proteins similar to Mycobacterium tuberculosis AhpE. AhpE is described as a 1-cys PRX because of the absence of a resolving cysteine. The structure and sequence of AhpE, however, show greater similarity to 2-cys PRXs than 1-cys PRXs. PRXs are thiol-specific antioxidant (TSA) proteins that confer a protective role in cells through their peroxidase activity in which hydrogen peroxide, peroxynitrate, and organic hydroperoxides are reduced and detoxified using reducing equivalents derived from either thioredoxin, glutathione, trypanothione and AhpF. The first step of catalysis is the nucleophilic attack by the peroxidatic cysteine on the peroxide leading to the formation of a cysteine sulfenic acid intermediate. The absence of a resolving cysteine suggests that functional AhpE is regenerated by an external reductant. The solution behavior and crystal structure of AhpE show that it forms dimers and octamers.


Pssm-ID: 239316 [Multi-domain]  Cd Length: 149  Bit Score: 121.23  E-value: 7.77e-36
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1107030588   1 MKTGDTVADFELPDQTGTPRRLSVLLSDGPVVLFFYPAAMTPGCTKEACHFRDLAKEFAEVRASRVGISTDPVRKQAKFA 80
Cdd:cd03018     1 LEVGDKAPDFELPDQNGQEVRLSEFRGRKPVVLVFFPLAFTPVCTKELCALRDSLELFEAAGAEVLGISVDSPFSLRAWA 80

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1107030588  81 EVRRFDYPLLSD--AQGTVAAQFGVkrgLLGKLMPVKRTTFVIDTDRKV 127
Cdd:cd03018    81 EENGLTFPLLSDfwPHGEVAKAYGV---FDEDLGVAERAVFVIDRDGII 126
bcp PRK09437
thioredoxin-dependent thiol peroxidase; Reviewed
 1-130 2.55e-33

thioredoxin-dependent thiol peroxidase; Reviewed


Pssm-ID: 181857  Cd Length: 154  Bit Score: 114.65  E-value: 2.55e-33
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1107030588   1 MKTGDTVADFELPDQTGTPrrlsVLLSD---GPVVLFFYPAAMTPGCTKEACHFRDLAKEFAEVRASRVGISTDPVRKQA 77
Cdd:PRK09437    4 LKAGDIAPKFSLPDQDGEQ----VSLTDfqgQRVLVYFYPKAMTPGCTVQACGLRDNMDELKKAGVVVLGISTDKPEKLS 79

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*.
gi 1107030588  78 KFAEVRRFDYPLLSDAQGTVAAQFGV--KRGLLGKLMP-VKRTTFVIDTDRKVLDV 130
Cdd:PRK09437   80 RFAEKELLNFTLLSDEDHQVAEQFGVwgEKKFMGKTYDgIHRISFLIDADGKIEHV 135
Redoxin pfam08534
Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.
 2-131 3.36e-17

Redoxin; This family of redoxins includes peroxiredoxin, thioredoxin and glutaredoxin proteins.


Pssm-ID: 400717 [Multi-domain]  Cd Length: 148  Bit Score: 73.17  E-value: 3.36e-17
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1107030588   2 KTGDTVADFELPDQTGTPRRLSvlLSD---GPVVLFFYPAAMTPGCTKEACHFRDLAKEFAEVRASRVGISTDPVRK-QA 77
Cdd:pfam08534   1 KAGDKAPDFTLPDAATDGNTVS--LSDfkgKKVVLNFWPGAFCPTCSAEHPYLEKLNELYKEKGVDVVAVNSDNDAFfVK 78

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....
gi 1107030588  78 KFAEVRRFDYPLLSDAQGTVAAQFGVKRGLLGKLMPVKRTTFVIDTDRKVLDVI 131
Cdd:pfam08534  79 RFWGKEGLPFPFLSDGNAAFTKALGLPIEEDASAGLRSPRYAVIDEDGKVVYLF 132
TrxA COG0526
Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, ...
 1-150 7.64e-15

Thiol-disulfide isomerase or thioredoxin [Posttranslational modification, protein turnover, chaperones];


Pssm-ID: 440292 [Multi-domain]  Cd Length: 139  Bit Score: 67.02  E-value: 7.64e-15
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1107030588   1 MK-TGDTVADFELPDQTGTPRRLSVLlSDGPVVLFFYpAAMTPGCTKEACHFRDLAKEFAEVRAsrVGISTDPVRKQAK- 78
Cdd:COG0526     1 MKaVGKPAPDFTLTDLDGKPLSLADL-KGKPVLVNFW-ATWCPPCRAEMPVLKELAEEYGGVVF--VGVDVDENPEAVKa 76

                          90       100       110       120       130       140       150
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1107030588  79 FAEVRRFDYPLLSDAQGTVAAQFGVKRgllgklMPvkrTTFVIDTDRKVLDVISSEFSMDAhADKALATLRA 150
Cdd:COG0526    77 FLKELGLPYPVLLDPDGELAKAYGVRG------IP---TTVLIDKDGKIVARHVGPLSPEE-LEEALEKLLA 138
PRX_like2 cd02970
Peroxiredoxin (PRX)-like 2 family; hypothetical proteins that show sequence similarity to PRXs. ...
 6-128 1.18e-14

Peroxiredoxin (PRX)-like 2 family; hypothetical proteins that show sequence similarity to PRXs. Members of this group contain a CXXC motif, similar to TRX. The second cysteine in the motif corresponds to the peroxidatic cysteine of PRX, however, these proteins do not contain the other two residues of the catalytic triad of PRX. PRXs confer a protective antioxidant role in cells through their peroxidase activity in which hydrogen peroxide, peroxynitrate, and organic hydroperoxides are reduced and detoxified using reducing equivalents derived from either thioredoxin, glutathione, trypanothione and AhpF. TRXs alter the redox state of target proteins by catalyzing the reduction of their disulfide bonds via the CXXC motif using reducing equivalents derived from either NADPH or ferredoxins.


Pssm-ID: 239268 [Multi-domain]  Cd Length: 149  Bit Score: 66.61  E-value: 1.18e-14
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1107030588   6 TVADFELPDQTGTPRRLSVLLSDGPVVLFFYpaaMTPGCTKEACHFRDLAKEFAEVRASR---VGISTDPVRKQAKFAEV 82
Cdd:cd02970     1 TAPDFELPDAGGETVTLSALLGEGPVVVVFY---RGFGCPFCREYLRALSKLLPELDALGvelVAVGPESPEKLEAFDKG 77

                          90       100       110       120       130       140
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 1107030588  83 RRFDYPLLSDAQGTVAAQFGVKRGLL-----GKLMPVKRT---------------TFVIDTDRKVL 128
Cdd:cd02970    78 KFLPFPVYADPDRKLYRALGLVRSLPwsntpRALWKNAAIgfrgndegdglqlpgVFVIGPDGTIL 143
AhpC COG0450
Alkyl hydroperoxide reductase subunit AhpC (peroxiredoxin) [Defense mechanisms];
31-127 4.91e-13

Alkyl hydroperoxide reductase subunit AhpC (peroxiredoxin) [Defense mechanisms];


Pssm-ID: 440219  Cd Length: 196  Bit Score: 63.17  E-value: 4.91e-13
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1107030588  31 VVLFFYPAAMTPGCTKEACHFRDLAKEFAEVRASRVGISTDPV----------RKQAKFAEVrrfDYPLLSDAQGTVAAQ 100
Cdd:COG0450    35 VVLFFHPADFTFVCPTELGAFAKRYEEFKKLGVEVIGLSVDSVfshkawhetiKEKGGIVKI---KFPIIADPTGKIARA 111

                          90       100       110
                  ....*....|....*....|....*....|..
gi 1107030588 101 FGVkrgllgkLMP-----VkRTTFVIDTDRKV 127
Cdd:COG0450   112 YGM-------LHPedgvaV-RGVFIIDPDGKI 135
TlpA_like_family cd02966
TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are ...
 9-132 3.47e-11

TlpA-like family; composed of TlpA, ResA, DsbE and similar proteins. TlpA, ResA and DsbE are bacterial protein disulfide reductases with important roles in cytochrome maturation. They are membrane-anchored proteins with a soluble TRX domain containing a CXXC motif located in the periplasm. The TRX domains of this family contain an insert, approximately 25 residues in length, which correspond to an extra alpha helix and a beta strand when compared with TRX. TlpA catalyzes an essential reaction in the biogenesis of cytochrome aa3, while ResA and DsbE are essential proteins in cytochrome c maturation. Also included in this family are proteins containing a TlpA-like TRX domain with domain architectures similar to E. coli DipZ protein, and the N-terminal TRX domain of PilB protein from Neisseria which acts as a disulfide reductase that can recylce methionine sulfoxide reductases.


Pssm-ID: 239264 [Multi-domain]  Cd Length: 116  Bit Score: 56.86  E-value: 3.47e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1107030588   9 DFELPDQTGTPRRLSVLLsDGPVVLFFYpAAMTPGCTKEACHFRDLAKEFAEVRASRVGISTDPVRKQA--KFAEVRRFD 86
Cdd:cd02966     1 DFSLPDLDGKPVSLSDLK-GKVVLVNFW-ASWCPPCRAEMPELEALAKEYKDDGVEVVGVNVDDDDPAAvkAFLKKYGIT 78

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*.
gi 1107030588  87 YPLLSDAQGTVAAQFGVKRgllgklMPvkrTTFVIDTDRKVLDVIS 132
Cdd:cd02966    79 FPVLLDPDGELAKAYGVRG------LP---TTFLIDRDGRIRARHV 115
PRX_1cys cd03016
Peroxiredoxin (PRX) family, 1-cys PRX subfamily; composed of PRXs containing only one ...
 4-127 4.17e-11

Peroxiredoxin (PRX) family, 1-cys PRX subfamily; composed of PRXs containing only one conserved cysteine, which serves as the peroxidatic cysteine. They are homodimeric thiol-specific antioxidant (TSA) proteins that confer a protective role in cells by reducing and detoxifying hydrogen peroxide, peroxynitrite, and organic hydroperoxides. As with all other PRXs, a cysteine sulfenic acid intermediate is formed upon reaction of 1-cys PRX with its substrates. Having no resolving cysteine, the oxidized enzyme is resolved by an external small-molecule or protein reductant such as thioredoxin or glutaredoxin. Similar to typical 2-cys PRX, 1-cys PRX forms a functional dimeric unit with a B-type interface, as well as a decameric structure which is stabilized in the reduced form of the enzyme. Other oligomeric forms, tetramers and hexamers, have also been reported. Mammalian 1-cys PRX is localized cellularly in the cytosol and is expressed at high levels in brain, eye, testes and lung. The seed-specific plant 1-cys PRXs protect tissues from reactive oxygen species during desiccation and are also called rehydrins.


Pssm-ID: 239314  Cd Length: 203  Bit Score: 58.32  E-value: 4.17e-11
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1107030588   4 GDTVADFELpDQTGTPRRLSVLLSDGPVVLFFYPAAMTPGCTKEACHFRDLAKEFAEVRASRVGISTDPVRKQAKFAE-- 81
Cdd:cd03016     2 GDTAPNFEA-DTTHGPIKFHDYLGDSWGILFSHPADFTPVCTTELGAFAKLAPEFKKRNVKLIGLSVDSVESHIKWIEdi 80

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|
gi 1107030588  82 ----VRRFDYPLLSDAQGTVAAQFGVKRGLLGKLMPVkRTTFVIDTDRKV 127
Cdd:cd03016    81 eeytGVEIPFPIIADPDREVAKLLGMIDPDAGSTLTV-RAVFIIDPDKKI 129
PRX_Typ2cys cd03015
Peroxiredoxin (PRX) family, Typical 2-Cys PRX subfamily; PRXs are thiol-specific antioxidant ...
 31-127 1.13e-10

Peroxiredoxin (PRX) family, Typical 2-Cys PRX subfamily; PRXs are thiol-specific antioxidant (TSA) proteins, which confer a protective role in cells through its peroxidase activity by reducing hydrogen peroxide, peroxynitrite, and organic hydroperoxides. The functional unit of typical 2-cys PRX is a homodimer. A unique intermolecular redox-active disulfide center is utilized for its activity. Upon reaction with peroxides, its peroxidatic cysteine is oxidized into a sulfenic acid intermediate which is resolved by bonding with the resolving cysteine from the other subunit of the homodimer. This intermolecular disulfide bond is then reduced by thioredoxin, tryparedoxin or AhpF. Typical 2-cys PRXs, like 1-cys PRXs, form decamers which are stabilized by reduction of the active site cysteine. Typical 2-cys PRX interacts through beta strands at one edge of the monomer (B-type interface) to form the functional homodimer, and uses an A-type interface (similar to the dimeric interface in atypical 2-cys PRX and PRX5) at the opposite end of the monomer to form the stable decameric (pentamer of dimers) structure.


Pssm-ID: 239313  Cd Length: 173  Bit Score: 56.74  E-value: 1.13e-10
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1107030588  31 VVLFFYPAAMTPGCTKEACHFRDLAKEFAEVRASRVGISTDPV----------RKQAKFAEVRrfdYPLLSDAQGTVAAQ 100
Cdd:cd03015    32 VVLFFYPLDFTFVCPTEIIAFSDRYEEFKKLNAEVLGVSTDSHfshlawrntpRKEGGLGKIN---FPLLADPKKKISRD 108

                          90       100       110
                  ....*....|....*....|....*....|
gi 1107030588 101 FGV---KRGLlgklmpVKRTTFVIDTDRKV 127
Cdd:cd03015   109 YGVldeEEGV------ALRGTFIIDPEGII 132
PRK13599 PRK13599
peroxiredoxin;
32-154 1.74e-09

peroxiredoxin;


Pssm-ID: 106544 [Multi-domain]  Cd Length: 215  Bit Score: 54.33  E-value: 1.74e-09
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1107030588  32 VLFFYPAAMTPGCTKEACHFRDLAKEFAEVRASRVGISTDPVRKQAKFAEVRR------FDYPLLSDAQGTVAAQFGVKR 105
Cdd:PRK13599   32 VLFSHPADFTPVCTTEFVEFARKANDFKELNTELIGLSVDQVFSHIKWVEWIKdntniaIPFPVIADDLGKVSNQLGMIH 111

                          90       100       110       120
                  ....*....|....*....|....*....|....*....|....*....
gi 1107030588 106 GllGKLMPVKRTTFVIDTDRKVLDVISSEFSMDAHADKALATLRAIRSG 154
Cdd:PRK13599  112 P--GKGTNTVRAVFIVDDKGTIRLIMYYPQEVGRNVDEILRALKALQTA 158
PRK13189 PRK13189
peroxiredoxin; Provisional
 31-127 5.21e-07

peroxiredoxin; Provisional


Pssm-ID: 237297  Cd Length: 222  Bit Score: 47.28  E-value: 5.21e-07
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1107030588  31 VVLFFYPAAMTPGCTKEACHFRDLAKEFAEVRASRVGISTDPVRKQAKFAE-------VrRFDYPLLSDAQGTVAaqfgv 103
Cdd:PRK13189   38 FVLFSHPADFTPVCTTEFVAFQKRYDEFRELNTELIGLSIDQVFSHIKWVEwikeklgV-EIEFPIIADDRGEIA----- 111

                          90       100
                  ....*....|....*....|....*....
gi 1107030588 104 krGLLGKLMPVKRTT-----FVIDTDRKV 127
Cdd:PRK13189  112 --KKLGMISPGKGTNtvravFIIDPKGII 138
PTZ00253 PTZ00253
tryparedoxin peroxidase; Provisional
 31-152 1.02e-06

tryparedoxin peroxidase; Provisional


Pssm-ID: 140280  Cd Length: 199  Bit Score: 46.44  E-value: 1.02e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1107030588  31 VVLFFYPAAMTPGCTKEACHFRDLAKEFAEVRASRVGISTDPVRKQAKFAEVRR-------FDYPLLSDAQGTVAAQFGV 103
Cdd:PTZ00253   39 VVLFFYPLDFTFVCPTEIIQFSDSVKRFNELNCEVLACSMDSEYAHLQWTLQERkkgglgtMAIPMLADKTKSIARSYGV 118

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|..
gi 1107030588 104 ---KRGLlgklmpVKRTTFVIDTDRKVLDVISSEFSMDAHADKALATLRAIR 152
Cdd:PTZ00253  119 leeEQGV------AYRGLFIIDPKGMLRQITVNDMPVGRNVEEVLRLLEAFQ 164
PRX_like1 cd02969
Peroxiredoxin (PRX)-like 1 family; hypothetical proteins that show sequence similarity to PRXs. ...
 4-128 1.31e-06

Peroxiredoxin (PRX)-like 1 family; hypothetical proteins that show sequence similarity to PRXs. Members of this group contain a conserved cysteine that aligns to the first cysteine in the CXXC motif of TRX. This does not correspond to the peroxidatic cysteine found in PRXs, which aligns to the second cysteine in the CXXC motif of TRX. In addition, these proteins do not contain the other two conserved residues of the catalytic triad of PRX. PRXs confer a protective antioxidant role in cells through their peroxidase activity in which hydrogen peroxide, peroxynitrate, and organic hydroperoxides are reduced and detoxified using reducing equivalents derived from either thioredoxin, glutathione, trypanothione and AhpF.


Pssm-ID: 239267 [Multi-domain]  Cd Length: 171  Bit Score: 45.69  E-value: 1.31e-06
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1107030588   4 GDTVADFELPDQTGTPRRLSVLLSDGPVVLFFypaaMTPGC---TKEACHFRDLAKEFAEVRASRVGISTDPVRKQ---- 76
Cdd:cd02969     1 GSPAPDFSLPDTDGKTYSLADFADGKALVVMF----ICNHCpyvKAIEDRLNRLAKEYGAKGVAVVAINSNDIEAYpeds 76

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1107030588  77 ----AKFAEVRRFDYPLLSDAQGTVAAQFGVKRgllgklmpvkrtT---FVIDTDRKVL 128
Cdd:cd02969    77 penmKAKAKEHGYPFPYLLDETQEVAKAYGAAC------------TpdfFLFDPDGKLV 123
PTZ00137 PTZ00137
2-Cys peroxiredoxin; Provisional
 23-152 1.70e-04

2-Cys peroxiredoxin; Provisional


Pssm-ID: 173427  Cd Length: 261  Bit Score: 40.32  E-value: 1.70e-04
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1107030588  23 SVLLSDGPVVLFFYPAAMTPGCTKEACHFRDLAKEFAEVRASRVGISTDPVRKQAKFAE-------VRRFDYPLLSDAQG 95
Cdd:PTZ00137   93 SDYFKDSYGLLVFYPLDFTFVCPSELLGFSERLKEFEERGVKVLGVSVDSPFSHKAWKEldvrqggVSPLKFPLFSDISR 172

                          90       100       110       120       130
                  ....*....|....*....|....*....|....*....|....*....|....*....
gi 1107030588  96 TVAAQFGVKR--GLlgklmpVKRTTFVIDTDRKVLDVISSEFSMDAHADKALATLRAIR 152
Cdd:PTZ00137  173 EVSKSFGLLRdeGF------SHRASVLVDKAGVVKHVAVYDLGLGRSVDETLRLFDAVQ 225
PRK13190 PRK13190
putative peroxiredoxin; Provisional
 31-127 2.46e-03

putative peroxiredoxin; Provisional


Pssm-ID: 106159  Cd Length: 202  Bit Score: 36.75  E-value: 2.46e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1107030588  31 VVLFFYPAAMTPGCTKEACHFRDLAKEFAEVRASRVGISTDPVrkQAKFAEVR----RF----DYPLLSDAQGTVAAQFG 102
Cdd:PRK13190   30 VLLFSHPADFTPVCTTEFIAFSRRYEDFKKLGVELVGLSVDSI--YSHIAWLRdieeRFgikiPFPVIADIDKELAREYN 107

                          90       100
                  ....*....|....*....|....*
gi 1107030588 103 VKRGLLGKLMpvkRTTFVIDTDRKV 127
Cdd:PRK13190  108 LIDENSGATV---RGVFIIDPNQIV 129
PRK10382 PRK10382
alkyl hydroperoxide reductase subunit C; Provisional
 32-124 3.35e-03

alkyl hydroperoxide reductase subunit C; Provisional


Pssm-ID: 182423  Cd Length: 187  Bit Score: 36.12  E-value: 3.35e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1107030588  32 VLFFYPAAMTPGCTKEACHFRDLAKEFAEVRASRVGISTDP--VRK--QAKFAEVRRFDYPLLSDAQGTVAAQFGVKRGL 107
Cdd:PRK10382   35 VFFFYPADFTFVCPTELGDVADHYEELQKLGVDVYSVSTDThfTHKawHSSSETIAKIKYAMIGDPTGALTRNFDNMRED 114

                          90
                  ....*....|....*..
gi 1107030588 108 LGKlmpVKRTTFVIDTD 124
Cdd:PRK10382  115 EGL---ADRATFVVDPQ 128
PRK13191 PRK13191
putative peroxiredoxin; Provisional
 32-103 5.20e-03

putative peroxiredoxin; Provisional


Pssm-ID: 183885  Cd Length: 215  Bit Score: 35.98  E-value: 5.20e-03
                          10        20        30        40        50        60        70        80
                  ....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1107030588  32 VLFFYPAAMTPGCTKEACHFRDLAKEFAEVRASRVGISTDP----------VRKQAKFaevrRFDYPLLSDAQGTVAAQF 101
Cdd:PRK13191   37 VLFSHPGDFTPVCTTEFYSFAKKYEEFKKLNTELIGLSVDSnishiewvmwIEKNLKV----EVPFPIIADPMGNVAKRL 112


                  ..
gi 1107030588 102 GV 103
Cdd:PRK13191  113 GM 114
 
Blast search parameters
Data Source: Precalculated data, version = cdd.v.3.21
Preset Options:Database: CDSEARCH/cdd   Low complexity filter: no  Composition Based Adjustment: yes   E-value threshold: 0.01

References:

  • Wang J et al. (2023), "The conserved domain database in 2023", Nucleic Acids Res.51(D)384-8.
  • Lu S et al. (2020), "The conserved domain database in 2020", Nucleic Acids Res.48(D)265-8.
  • Marchler-Bauer A et al. (2017), "CDD/SPARCLE: functional classification of proteins via subfamily domain architectures.", Nucleic Acids Res.45(D)200-3.
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